DNA sequence of the yeast transketolase gene

T. S. Fletcher, I. L. Kwee, Ingrid Kwee, C. Largman, B. M. Martin

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Transketolase (EC 2.2.1.1) is the enzyme that, together with aldolase, forms a reversible link between the glycolytic and pentose phosphate pathways. We have cloned and sequenced the transketolase gene from yeast (Saccharomyces cerevisiae). This is the first transketolase gene of the pentose phosphate shunt to be sequenced from any source. The molecular mass of the proposed translated protein is 73 976 daltons, in good agreement with the observed molecular mass of about 75 000 daltons. The 5'-nontranslated region of the gene is similar to other yeast genes. There is no evidence of 5'-splice junctions or branch points in the sequence. The 3'-nontranslated region contains the polyadenylation signal (AATAAA), 80 base pairs downstream from the termination codon. A high degree of homology is found between yeast transketolase and dihydroxyacetone synthase (formaldehyde transketolase) from the yeast Hansenula polymorpha. The overall sequence identity between these two proteins is 37%, with four regions of much greater similarity. The regions from amino acid residues 98-131, 157-182, 410-433, and 474-489 have sequence identities of 74%, 66%, 83%, and 82%, respectively. One of these regions (157-182) includes a possible thiamin pyrophosphate (TPP) binding domain, and another (410-433) may contain the catalytic domain.

Original languageEnglish (US)
Pages (from-to)1892-1896
Number of pages5
JournalBiochemistry
Volume31
Issue number6
StatePublished - 1992
Externally publishedYes

Fingerprint

Transketolase
formaldehyde transketolase
DNA sequences
Yeast
Genes
Yeasts
Pentose Phosphate Pathway
Pentoses
Molecular mass
Thiamine Pyrophosphate
Polyadenylation
Fructose-Bisphosphate Aldolase
Phosphates
Pichia
Terminator Codon
Base Pairing
Saccharomyces cerevisiae
Catalytic Domain
Proteins
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Fletcher, T. S., Kwee, I. L., Kwee, I., Largman, C., & Martin, B. M. (1992). DNA sequence of the yeast transketolase gene. Biochemistry, 31(6), 1892-1896.

DNA sequence of the yeast transketolase gene. / Fletcher, T. S.; Kwee, I. L.; Kwee, Ingrid; Largman, C.; Martin, B. M.

In: Biochemistry, Vol. 31, No. 6, 1992, p. 1892-1896.

Research output: Contribution to journalArticle

Fletcher, TS, Kwee, IL, Kwee, I, Largman, C & Martin, BM 1992, 'DNA sequence of the yeast transketolase gene', Biochemistry, vol. 31, no. 6, pp. 1892-1896.
Fletcher TS, Kwee IL, Kwee I, Largman C, Martin BM. DNA sequence of the yeast transketolase gene. Biochemistry. 1992;31(6):1892-1896.
Fletcher, T. S. ; Kwee, I. L. ; Kwee, Ingrid ; Largman, C. ; Martin, B. M. / DNA sequence of the yeast transketolase gene. In: Biochemistry. 1992 ; Vol. 31, No. 6. pp. 1892-1896.
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N2 - Transketolase (EC 2.2.1.1) is the enzyme that, together with aldolase, forms a reversible link between the glycolytic and pentose phosphate pathways. We have cloned and sequenced the transketolase gene from yeast (Saccharomyces cerevisiae). This is the first transketolase gene of the pentose phosphate shunt to be sequenced from any source. The molecular mass of the proposed translated protein is 73 976 daltons, in good agreement with the observed molecular mass of about 75 000 daltons. The 5'-nontranslated region of the gene is similar to other yeast genes. There is no evidence of 5'-splice junctions or branch points in the sequence. The 3'-nontranslated region contains the polyadenylation signal (AATAAA), 80 base pairs downstream from the termination codon. A high degree of homology is found between yeast transketolase and dihydroxyacetone synthase (formaldehyde transketolase) from the yeast Hansenula polymorpha. The overall sequence identity between these two proteins is 37%, with four regions of much greater similarity. The regions from amino acid residues 98-131, 157-182, 410-433, and 474-489 have sequence identities of 74%, 66%, 83%, and 82%, respectively. One of these regions (157-182) includes a possible thiamin pyrophosphate (TPP) binding domain, and another (410-433) may contain the catalytic domain.

AB - Transketolase (EC 2.2.1.1) is the enzyme that, together with aldolase, forms a reversible link between the glycolytic and pentose phosphate pathways. We have cloned and sequenced the transketolase gene from yeast (Saccharomyces cerevisiae). This is the first transketolase gene of the pentose phosphate shunt to be sequenced from any source. The molecular mass of the proposed translated protein is 73 976 daltons, in good agreement with the observed molecular mass of about 75 000 daltons. The 5'-nontranslated region of the gene is similar to other yeast genes. There is no evidence of 5'-splice junctions or branch points in the sequence. The 3'-nontranslated region contains the polyadenylation signal (AATAAA), 80 base pairs downstream from the termination codon. A high degree of homology is found between yeast transketolase and dihydroxyacetone synthase (formaldehyde transketolase) from the yeast Hansenula polymorpha. The overall sequence identity between these two proteins is 37%, with four regions of much greater similarity. The regions from amino acid residues 98-131, 157-182, 410-433, and 474-489 have sequence identities of 74%, 66%, 83%, and 82%, respectively. One of these regions (157-182) includes a possible thiamin pyrophosphate (TPP) binding domain, and another (410-433) may contain the catalytic domain.

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